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- W4200598839 abstract "Abstract In eukaryotic cells, stressors reprogram the cellular proteome by activating the integrated stress response (ISR). In its canonical form, stress-sensing kinases phosphorylate the eukaryotic translation initiation factor eIF2 (eIF2-P), which ultimately leads to reduced levels of ternary complex required for initiation of mRNA translation. Translational control is primarily exerted through a conformational switch in eIF2’s nucleotide exchange factor, eIF2B, which shifts from its active A-State conformation to its inhibited I-State conformation upon eIF2-P binding, resulting in reduced nucleotide exchange on eIF2. Here, we show functionally and structurally how a single histidine to aspartate point mutation in eIF2B’s β subunit (H160D) mimics the effects of eIF2-P binding by promoting an I-State like conformation, resulting in eIF2-P independent activation of the ISR. These findings corroborate our previously proposed (Schoof et al. 2021) A/I-State model of allosteric ISR regulation." @default.
- W4200598839 created "2021-12-31" @default.
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- W4200598839 date "2021-12-06" @default.
- W4200598839 modified "2023-09-28" @default.
- W4200598839 title "A point mutation in the nucleotide exchange factor eIF2B constitutively activates the integrated stress response by allosteric modulation" @default.
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- W4200598839 doi "https://doi.org/10.1101/2021.12.03.471181" @default.
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